Crystal structure analyses of uncomplexed ecotin in two crystal forms: Implications for its function and stability

Dong Hae Shin, Hyun Kyu Song, Ihn Sik Seong, Cheol Soon Lee, Chin Ha Chung, Se Won Suh

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that in complex with trypsin. Although there is no gross structural rearrangement of ecotin when binding trypsin, the loops involved in binding trypsin show relatively large shifts in atomic positions. The inherent flexibility of the loops and the highly nonglobular shape are the two features essential for its inhibitory function. An insight into the understanding of the structural basis of thermostability and acid stability of ecotin is also provided by the present structure.

Original languageEnglish
Pages (from-to)2236-2247
Number of pages12
JournalProtein Science
Volume5
Issue number11
DOIs
Publication statusPublished - 1996 Nov

Keywords

  • X-ray structure
  • ecotin
  • protease inhibitor
  • thermostability

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Crystal structure analyses of uncomplexed ecotin in two crystal forms: Implications for its function and stability'. Together they form a unique fingerprint.

  • Cite this